Cyclic Peptide Mimetic of Damaged Collagen
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acs.biomac.0c00103.pdf
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2.79 MB
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Author(s)
Ellison, Aubrey J.
Tanrikulu, Ismet Caglar
Dones-Monroig, Jesus M.
Raines, Ronald T
Date Issued
March 2020
Journal
Biomacromolecules
Publisher
American Chemical Society (ACS)
Citation
Aubrey J. Ellison, I. Caglar Tanrikulu, Jesús M. Dones, and Ronald T. Raines. "Cyclic Peptide Mimetic of Damaged Collagen." Biomacromolecules 2020 21 (4), 1539-1547. DOI: 10.1021/acs.biomac.0c00103.
Version
Final published version
Abstract
Collagen is the most abundant protein in humans and the major component of human skin. Collagen mimetic peptides (CMPs) can anneal to damaged collagen in vitro and in vivo. A duplex of CMPs was envisioned as a macromolecular mimic for damaged collagen. The duplex was synthesized on a solid support from the amino groups of a lysine residue and by using olefin metathesis to link the N termini. The resulting cyclic peptide, which is a monomer in solution, binds to CMPs to form a triple helix. Among these, CMPs that are engineered to avoid the formation of homotrimers but preorganized to adopt the conformation of a collagen strand exhibit enhanced association. Thus, this cyclic peptide enables the assessment of CMPs for utility in annealing to damaged collagen. Such CMPs have potential use in the diagnosis and treatment of fibrotic diseases and wounds.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.1021/acs.biomac.0c00103
